Row-like organization of ATP synthase in intact mitochondria determined by cryo-electron tomography
- authored by
- Natalya V. Dudkina, Gert T. Oostergetel, Dagmar Lewejohann, Hans Peter Braun, Egbert J. Boekema
- Abstract
The fine structure of intact, close-to-spherical mitochondria from the alga Polytomella was visualized by dual-axis cryo-electron tomography. The supramolecular organization of dimeric ATP synthase in the cristae membranes was investigated by averaging subvolumes of tomograms and 3D details at ∼ 6 nm resolution were revealed. Oligomeric ATP synthase is composed of rows of dimers at 12 nm intervals; the dimers make a slight angle along the row. In addition, the main features of monomeric ATP synthase, such as the conically shaped F1 headpiece, central stalk and stator were revealed. This demonstrates the capability of dual-axis electron tomography to unravel details of proteins and their interactions in complete organelles.
- Organisation(s)
-
Section Plant Molecular Biology and Plant Proteomics
Institute of Plant Genetics
- External Organisation(s)
-
University of Groningen
- Type
- Article
- Journal
- Biochimica et Biophysica Acta - Bioenergetics
- Volume
- 1797
- Pages
- 272-277
- No. of pages
- 6
- ISSN
- 0005-2728
- Publication date
- 17.11.2009
- Publication status
- Published
- Peer reviewed
- Yes
- ASJC Scopus subject areas
- Biophysics, Biochemistry, Cell Biology
- Electronic version(s)
-
https://doi.org/10.1016/j.bbabio.2009.11.004 (Access:
Open)
